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P46821 (MAP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein 1B

Short name=MAP-1B

Cleaved into the following 2 chains:

  1. MAP1B heavy chain
  2. MAP1 light chain LC1
Gene names
Name:MAP1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Facilitates tyrosination of alpha-tubulin in neuronal microtubules By similarity. Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. Ref.14

Subunit structure

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin tyrosine TTL By similarity. Interacts (via C-terminus) with GAN (via Kelch domains). Interacts (via N-terminus) with DAPK1. Interacts with TMEM185A. Interacts with MAP1LC3B. Ref.7 Ref.8 Ref.9 Ref.14 Ref.23

Subcellular location

Cytoplasmcytoskeleton. Cytoplasm. Cell junctionsynapse By similarity. Cell projectiondendritic spine By similarity. Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers By similarity. Ref.14

Domain

Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules.

Post-translational modification

LC1 is generated from MAP1B by proteolytic processing.

S-nitrosylation at Cys-2464 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction By similarity.

Sequence similarities

Belongs to the MAP1 family.

Ontologies

Keywords
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoskeleton
Microtubule
Synapse
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMAcetylation
Phosphoprotein
S-nitrosylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon extension

Inferred from electronic annotation. Source: Ensembl

cellular process

Inferred from direct assay PubMed 19567321. Source: DFLAT

dendrite development

Inferred from electronic annotation. Source: Ensembl

establishment of monopolar cell polarity

Inferred from electronic annotation. Source: Ensembl

microtubule bundle formation

Inferred from electronic annotation. Source: Ensembl

mitochondrion transport along microtubule

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Traceable author statement PubMed 1881920. Source: ProtInc

plasma membrane

Inferred from direct assay PubMed 19567321. Source: DFLAT

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Non-traceable author statement PubMed 1881920. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 24682467Microtubule-associated protein 1B
PRO_0000018604
Chain2 – 22062205MAP1B heavy chain
PRO_0000418379
Chain2207 – 2468262MAP1 light chain LC1
PRO_0000018605

Regions

Repeat1878 – 189417MAP1B 1
Repeat1895 – 191117MAP1B 2
Repeat1912 – 192817MAP1B 3
Repeat1929 – 194517MAP1B 4
Repeat1946 – 196217MAP1B 5
Repeat1963 – 197917MAP1B 6
Repeat1997 – 201317MAP1B 7
Repeat2014 – 203017MAP1B 8
Repeat2031 – 204717MAP1B 9
Repeat2048 – 206417MAP1B 10
Region2294 – 2468175Mediates interaction with TMEM185A
Compositional bias589 – 790202Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.22
Modified residue3361Phosphoserine Ref.12
Modified residue5411Phosphoserine By similarity
Modified residue5441Phosphoserine By similarity
Modified residue5611Phosphoserine By similarity
Modified residue6141Phosphoserine By similarity
Modified residue8281Phosphoserine Ref.22
Modified residue8311Phosphoserine Ref.20 Ref.22
Modified residue8321Phosphoserine Ref.20 Ref.22
Modified residue9371Phosphoserine Ref.22
Modified residue9921Phosphoserine Ref.10 Ref.22
Modified residue9951Phosphoserine Ref.10 Ref.22
Modified residue10161Phosphoserine Ref.10 Ref.17 Ref.22
Modified residue11441Phosphoserine Ref.22
Modified residue11541Phosphoserine Ref.22
Modified residue11561Phosphoserine Ref.22
Modified residue12081Phosphoserine Ref.22
Modified residue12521Phosphoserine Ref.22
Modified residue12561Phosphoserine Ref.22
Modified residue12601Phosphoserine Ref.22
Modified residue12651Phosphoserine Ref.10 Ref.22
Modified residue12761Phosphoserine Ref.10
Modified residue12801Phosphoserine Ref.10
Modified residue12821Phosphothreonine Ref.10 Ref.22
Modified residue13121Phosphoserine By similarity
Modified residue13781Phosphoserine Ref.22
Modified residue13871Phosphoserine Ref.22
Modified residue13891Phosphoserine Ref.22
Modified residue13961Phosphoserine Ref.10 Ref.20
Modified residue14001Phosphoserine Ref.10 Ref.20 Ref.22
Modified residue14271Phosphoserine Ref.10 Ref.15 Ref.22
Modified residue14381Phosphoserine Ref.10 Ref.22
Modified residue14431Phosphoserine Ref.10 Ref.22
Modified residue15011Phosphoserine Ref.20 Ref.22
Modified residue16181Phosphoserine Ref.10
Modified residue16201Phosphoserine Ref.10
Modified residue16251Phosphoserine Ref.10
Modified residue16531Phosphoserine Ref.22
Modified residue17791Phosphoserine Ref.10 Ref.19 Ref.22
Modified residue17821Phosphoserine Ref.10 Ref.22
Modified residue17851Phosphoserine Ref.22
Modified residue17881Phosphothreonine Ref.10 Ref.22
Modified residue17971Phosphoserine Ref.22
Modified residue19151Phosphoserine Ref.22
Modified residue19171Phosphoserine Ref.22
Modified residue19651Phosphoserine Ref.22
Modified residue22711Phosphoserine Ref.22
Modified residue22891Phosphoserine Ref.22
Modified residue24641S-nitrosocysteine By similarity

Natural variations

Natural variant3261R → Q in a colorectal cancer sample; somatic mutation. Ref.24
VAR_036016
Natural variant5741V → M in a colorectal cancer sample; somatic mutation. Ref.24
VAR_036017
Natural variant5941I → V. Ref.1 Ref.2 Ref.4
Corresponds to variant rs1866374 [ dbSNP | Ensembl ].
VAR_024530
Natural variant8691E → G.
Corresponds to variant rs16876070 [ dbSNP | Ensembl ].
VAR_030347
Natural variant12961P → L.
Corresponds to variant rs34093016 [ dbSNP | Ensembl ].
VAR_034105
Natural variant19171S → R.
Corresponds to variant rs13153166 [ dbSNP | Ensembl ].
VAR_056123

Sequences

Sequence LengthMass (Da)Tools
P46821 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 3FFDCB2E20049A8A

FASTA2,468270,634
        10         20         30         40         50         60 
MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE HLRRAIGNIE 

        70         80         90        100        110        120 
LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL HHRSDVLETV VLINPSDEAV 

       130        140        150        160        170        180 
STEVRLMITD AARHKLLVLT GQCFENTGEL ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP 

       190        200        210        220        230        240 
ANKASLTLFC PEEGDWKNSN LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP 

       250        260        270        280        290        300 
SPFDILEPPT SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 

       310        320        330        340        350        360 
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI SPDLGVVFLN 

       370        380        390        400        410        420 
VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIDPVI LFQKMGVGKL 

       430        440        450        460        470        480 
EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE FILPNGQEVD LPISYLTSVS SLIVWHPANP 

       490        500        510        520        530        540 
AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD 

       550        560        570        580        590        600 
SRESLKPAAK PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP 

       610        620        630        640        650        660 
SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK EEKEKPKKEV 

       670        680        690        700        710        720 
AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV KKETPPKEVK KEVKKEEKKE 

       730        740        750        760        770        780 
VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK KPAALKPKVP KKEESVKKDS VAAGKPKEKG 

       790        800        810        820        830        840 
KIKVIKKEGK AAEAVAAAVG TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF 

       850        860        870        880        890        900 
EELKAEEVDV TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE 

       910        920        930        940        950        960 
GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE AEEPEEDGEE 

       970        980        990       1000       1010       1020 
HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA EEDMDEAIEK GEAEQSEEEA 

      1030       1040       1050       1060       1070       1080 
DEEDKAEDAR EEEYEPEKME AEDYVMAVVD KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE 

      1090       1100       1110       1120       1130       1140 
PASSIHDETL PGGSESEATA SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR 

      1150       1160       1170       1180       1190       1200 
DVMSDETNNE ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY 

      1210       1220       1230       1240       1250       1260 
NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK VSPSKSPSLS 

      1270       1280       1290       1300       1310       1320 
PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE VTQEVVEEHC ASPEDKTLEV 

      1330       1340       1350       1360       1370       1380 
VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT EVIEKPPAVP VSFEFSDAKD ENERASVSPM 

      1390       1400       1410       1420       1430       1440 
DEPVPDSESP IEKVLSPLRS PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD 

      1450       1460       1470       1480       1490       1500 
QVSPVSEMTS TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV 

      1510       1520       1530       1540       1550       1560 
SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA SVSTASVATS 

      1570       1580       1590       1600       1610       1620 
SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT FQETEMSPSK EECPRPMSIS 

      1630       1640       1650       1660       1670       1680 
PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG QESPEQSLAM DFSRQSPDHP TVGAGVLHIT 

      1690       1700       1710       1720       1730       1740 
ENGPTEVDYS PSDMQDSSLS HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ 

      1750       1760       1770       1780       1790       1800 
IASPLQEDTL SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF 

      1810       1820       1830       1840       1850       1860 
SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD LSTPGLEKDS 

      1870       1880       1890       1900       1910       1920 
GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD VGGYYYEKIE RTTKSPSDSG 

      1930       1940       1950       1960       1970       1980 
YSYETIGKTT KTPEDGDYSY EIIEKTTRTP EEGGYSYDIS EKTTSPPEVS GYSYEKTERS 

      1990       2000       2010       2020       2030       2040 
RRLLDDISNG YDDSEDGGHT LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY 

      2050       2060       2070       2080       2090       2100 
CYETAEKITR TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS 

      2110       2120       2130       2140       2150       2160 
FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV SESAPSQTDS 

      2170       2180       2190       2200       2210       2220 
DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP PPAPVQDRSP SPRHPDVSMV 

      2230       2240       2250       2260       2270       2280 
DPEALAIEQN LGKALKKDLK EKTKTKKPGT KTKSSSPVKK SDGKSKPLAA SPKPAGLKES 

      2290       2300       2310       2320       2330       2340 
SDKVSRVASP KKKESVEKAA KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG 

      2350       2360       2370       2380       2390       2400 
TTKTTKSSAV PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA 

      2410       2420       2430       2440       2450       2460 
VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS SSTVVMQDES 


FPACKIEL 

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References

« Hide 'large scale' references
[1]"Cloning of human microtubule-associated protein 1B and the identification of a related gene on chromosome 15."
Lien L.L., Feener C., Fischbach N., Kunkel L.M.
Genomics 22:273-280(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
Tissue: Fetal brain.
[2]"Hmob3 brain-specific sequence is a part of phylogenetically conserved human MAP1B gene 3'-untranslated region."
Dergunova L.V., Raevskaya N.M., Vladychenskaya I.P., Limborska S.A.
Biomol. Eng. 20:91-96(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-594.
[5]Bienvenut W.V., Pchelintsev N., Adams P.D.
Submitted (OCT-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-31; 55-64; 90-98; 391-429; 520-531; 1052-1070; 1233-1250; 1276-1287; 1462-1476; 1834-1958 AND 1898-1908, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Lung fibroblast.
[6]Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2347-2370 AND 2382-2409, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"Microtubule-associated protein 1B: a neuronal binding partner for gigaxonin."
Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A., Yang Y.
J. Cell Biol. 158:427-433(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAN.
[8]"Cloning of a novel neuronally expressed orphan G-protein-coupled receptor which is up-regulated by erythropoietin, interacts with microtubule-associated protein 1b and colocalizes with the 5-hydroxytryptamine 2a receptor."
Maurer M.H., Gruenewald S., Gassler N., Rossner M., Propst F., Wuerz R., Weber D., Kuner T., Kuschinsky W., Schneider A.
J. Neurochem. 91:1007-1017(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM185A.
[9]"Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival."
Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.
Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAN.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-995; SER-1016; SER-1265; SER-1276; SER-1280; THR-1282; SER-1396; SER-1400; SER-1427; SER-1438; SER-1443; SER-1618; SER-1620; SER-1625; SER-1779; SER-1782 AND THR-1788, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site."
Zou B., Yan H., Kawasaki F., Ordway R.W.
Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE SITE.
[14]"DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing."
Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P., Hupp T.R.
J. Biol. Chem. 283:9999-10014(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.
[15]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-832; SER-1396; SER-1400 AND SER-1501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828; SER-831; SER-832; SER-937; SER-992; SER-995; SER-1016; SER-1144; SER-1154; SER-1156; SER-1208; SER-1252; SER-1256; SER-1260; SER-1265; THR-1282; SER-1378; SER-1387; SER-1389; SER-1400; SER-1427; SER-1438; SER-1443; SER-1501; SER-1653; SER-1779; SER-1782; SER-1785; THR-1788; SER-1797; SER-1915; SER-1917; SER-1965; SER-2271 AND SER-2289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1LC3B.
[24]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-326 AND MET-574.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06237 mRNA. Translation: AAA18904.1.
BN001084 mRNA. Translation: CAM06633.1.
AC012609 Genomic DNA. No translation available.
AC093218 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95697.1.
RefSeqNP_005900.2. NM_005909.3.
UniGeneHs.335079.

3D structure databases

ProteinModelPortalP46821.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110304. 40 interactions.
DIPDIP-33474N.
IntActP46821. 27 interactions.
MINTMINT-243072.
STRING9606.ENSP00000296755.

PTM databases

PhosphoSiteP46821.

Polymorphism databases

DMDM317373388.

Proteomic databases

PaxDbP46821.
PRIDEP46821.

Protocols and materials databases

DNASU4131.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296755; ENSP00000296755; ENSG00000131711.
GeneID4131.
KEGGhsa:4131.
UCSCuc003kbw.4. human.

Organism-specific databases

CTD4131.
GeneCardsGC05P071438.
HGNCHGNC:6836. MAP1B.
HPACAB009792.
HPA022275.
MIM157129. gene.
neXtProtNX_P46821.
PharmGKBPA30581.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000063256.
HOVERGENHBG052409.
InParanoidP46821.
KOK10429.
OMARTPVQDH.
OrthoDBEOG773XKP.
PhylomeDBP46821.
TreeFamTF350229.

Gene expression databases

ArrayExpressP46821.
BgeeP46821.
CleanExHS_MAP1B.
GenevestigatorP46821.

Family and domain databases

Gene3D3.60.15.10. 2 hits.
InterProIPR001279. Beta-lactamas-like.
IPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
[Graphical view]
PANTHERPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamPF00414. MAP1B_neuraxin. 5 hits.
[Graphical view]
PROSITEPS00230. MAP1B_NEURAXIN. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAP1B. human.
GeneWikiMAP1B.
GenomeRNAi4131.
NextBio16218.
PROP46821.
SOURCESearch...

Entry information

Entry nameMAP1B_HUMAN
AccessionPrimary (citable) accession number: P46821
Secondary accession number(s): A2BDK5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM